ID B0W052_CULQU Unreviewed; 930 AA.
AC B0W052;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 92.
DE SubName: Full=Alpha-aminoadipic semialdehyde synthase, mitochondrial {ECO:0000313|EMBL:EDS37624.1};
GN Name=6031256 {ECO:0000313|EnsemblMetazoa:CPIJ000416-PA};
GN ORFNames=CpipJ_CPIJ000416 {ECO:0000313|EMBL:EDS37624.1};
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1] {ECO:0000313|EMBL:EDS37624.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB {ECO:0000313|EMBL:EDS37624.1};
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:CPIJ000416-PA}
RP IDENTIFICATION.
RC STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ000416-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC pathway; glutaryl-CoA from L-lysine: step 1/6.
CC {ECO:0000256|ARBA:ARBA00004682}.
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC pathway; glutaryl-CoA from L-lysine: step 2/6.
CC {ECO:0000256|ARBA:ARBA00004720}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the saccharopine
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00025744}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AlaDH/PNT family.
CC {ECO:0000256|ARBA:ARBA00005624}.
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DR EMBL; DS231816; EDS37624.1; -; Genomic_DNA.
DR RefSeq; XP_001842086.1; XM_001842034.1.
DR AlphaFoldDB; B0W052; -.
DR STRING; 7176.B0W052; -.
DR EnsemblMetazoa; CPIJ000416-RA; CPIJ000416-PA; CPIJ000416.
DR GeneID; 6031256; -.
DR KEGG; cqu:CpipJ_CPIJ000416; -.
DR VEuPathDB; VectorBase:CPIJ000416; -.
DR VEuPathDB; VectorBase:CQUJHB015500; -.
DR eggNOG; KOG0172; Eukaryota.
DR HOGENOM; CLU_005231_0_1_1; -.
DR InParanoid; B0W052; -.
DR OMA; TPHVHDI; -.
DR OrthoDB; 2184985at2759; -.
DR UniPathway; UPA00868; UER00835.
DR Proteomes; UP000002320; Unassembled WGS sequence.
DR GO; GO:0047131; F:saccharopine dehydrogenase (NAD+, L-glutamate-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0047130; F:saccharopine dehydrogenase (NADP+, L-lysine-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
DR CDD; cd12189; LKR_SDH_like; 1.
DR Gene3D; 1.10.1870.10; Domain 3, Saccharopine reductase; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
DR InterPro; IPR007886; AlaDH/PNT_N.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032095; Sacchrp_dh-like_C.
DR InterPro; IPR005097; Sacchrp_dh_NADP.
DR PANTHER; PTHR11133:SF25; ALPHA-AMINOADIPIC SEMIALDEHYDE SYNTHASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11133; SACCHAROPINE DEHYDROGENASE; 1.
DR Pfam; PF05222; AlaDh_PNT_N; 1.
DR Pfam; PF16653; Sacchrp_dh_C; 1.
DR Pfam; PF03435; Sacchrp_dh_NADP; 1.
DR SMART; SM01002; AlaDh_PNT_C; 1.
DR SMART; SM01003; AlaDh_PNT_N; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002320}.
FT DOMAIN 27..157
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 197..400
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 930 AA; 103010 MW; 54EA6FE6BA3CC5D0 CRC64;
MFRILKCRET LSPRLFYRAK HSGKVIAIRR EDQSVWERRA SFSPVIVKKL IKQGVKVIVQ
PSNRRAYPMQ AYLNAGATVQ EDISEASVIF GVKQVPVDAL IPQKTYCFFS HTIKAQESNM
PLLDACLEKN IRLIDYEKLM DRNGQRLVAF GKYAGVAGMI NILHGIGLRM LALGHHTPFM
HVGPAHNYRN SSMARQAVRD CGYEIALGMM PKSIGPLTFI FTGSGNVSQG AQEVFQELPI
EFVPPDSLRK VAEHGSQNKL YGCEVSRADH LERREGGGFD PVEYDQYPER YISTFNKKIA
PYASVIINGI YWAVGSPKLI TIPDAKNLLR PADTPWLPTS RGAPALPHRM LAICDISADP
GGSIEFMNEC TTIDTPFCLY DADRNKDQKS FKGPGVLVCS IDNMPTQLPR ESTDFFGELL
YPYALDILQS DATKPLEDHK FCQPVEGAII CSNGQLTTGF EYINELRESN NRSRHKSEGS
SVGKKRVLVL GAGFVSAPLV EYLHREGNVS IKVGSQIKEE ADRLANRYQG IESVYINVED
ESANLQNLCE ESDVVVSLLP YALHGLIAKH CVAGRTHLVT ASYLNDDIKA LHESARDAGV
TLMNEVGLDP GIDHLLALDC IQEVQEKGGT VESFVSFCGG LPAPEHSDNP LRYKFSWSPR
GVLLNTLSAA KYLSKGQVVE ISGGGELLTV PRELEFLPGF ALEGFPNRDS TKYQELYGLS
NVHTLLRGTI RYKGFSDNIK PMQLLGLIDP NPHPLLHPHG PELTWRQLVI NLLGLVDAEI
FYENLRIKLA ERVGNLEGIE ELGLLDNTPV VKMGSPLDTL SHYLSKKLAF ANTERDLIVL
RHDVGIRWSD GRREERGINF VAYGQPAING GHSAMAVTVG FPAAIATKMI LDGEIQQRGV
VLPFTSDIYR PMLARLENEG LVATTTSKML
//
